Conformations of immunoglobulin hypervariable regions

Cyrus Chothia (1, 2) , Arthur Lesk (1, 3) , Anna Tramontano (3) , Michael Levitt (4, 1, 5) , Sandra Smith-Gill (6) , Gillian Air (7) , Steven Sheriff (6) , Eduardo Padlan (6) , David Davies (6) , William Tulip (8) , Peter Colman (8) , Silvia Spinelli (9) , Pedro Alzari (9) , Roberto Poljak (9)

1 LMB - MRC Laboratory of Molecular Biology [Cambridge, UK]
2 UCL - University College of London [London]
3 EMBL - European Molecular Biology Laboratory [Heidelberg]
4 Department of Structural Biology [Stanford]
5 Stanford University
6 NIH - National Institutes of Health [Bethesda]
7 UA - University of Alabama [Tuscaloosa]
8 CSIRO Energy Technology - Commonwealth Scientific and Industrial Research Organisation Energy Technology
9 Immunologie structurale

On the basis of comparative studies of known antibody structures and sequences it has been argued that there is a small repertoire of main-chain conformations for at least five of the six hypervariable regions of antibodies, and that the particular conformation adopted is determined by a few key conserved residues. These hypotheses are now supported by reasonably successful predictions of the structures of most hypervariable regions of various antibodies, as revealed by comparison with their subsequently determined structures.

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Cyrus Chothia, Arthur Lesk, Anna Tramontano, Michael Levitt, Sandra Smith-Gill, et al.. Conformations of immunoglobulin hypervariable regions. Nature, 1989, 342 (6252), pp.877-883. ⟨10.1038/342877a0⟩. ⟨pasteur-03136436⟩